Nonequilibrium antifreeze peptides and the recrystallization of ice. 1995

C A Knight, and D Wen, and R A Laursen
National Center for Atmospheric Research, Boulder, Colorado 80307.

Evidence is presented that the nonequilibrium antifreeze peptide (AFP) from winter flounder has a special ability to inhibit recrystallization in ice only when an appreciable amount of liquid is present, as is the case when the system contains salts and the temperature is not too low. In this circumstance the AFP binds to the ice surface at the ice-solution interfaces in grain boundaries, preventing migration of the solution and effectively immobilizing the boundaries. In the absence of liquid, recrystallization inhibition appears to be a common property of many peptides. This is consistent with the view that the special effects of AFPs require a structural fit onto ice, and therefore require the AFP molecules to have the mobility to achieve that fit. Since the concentration of salt required to induce the special recrystallization inhibition effects of AFPs is lower (< 10 mM) than that found normally in physiological fluids, AFPs could play a role in the survival of organisms by preventing damage due to recrystallization. The proposition that mobility is needed for AFP molecules to produce their special influence upon ice growth argues against any special effects of AFPs in devitrification.

UI MeSH Term Description Entries
D007053 Ice The solid substance formed by the FREEZING of water.
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D005432 Flounder Common name for two families of FLATFISHES belonging to the order Pleuronectiformes: left-eye flounders (Bothidae) and right-eye flounders (Pleuronectidae). The latter is more commonly used in research. Plaice,Platichthys,Pleuronectes,Pseudopleuronectes,Halibut,Pleuronectes platessa,Flounders
D005615 Freezing Liquids transforming into solids by the removal of heat. Melting
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017421 Sequence Analysis A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information. Sequence Determination,Analysis, Sequence,Determination, Sequence,Determinations, Sequence,Sequence Determinations,Analyses, Sequence,Sequence Analyses
D021301 Antifreeze Proteins Proteins that bind to ice and modify the growth of ice crystals. They perform a cryoprotective role in a variety of organisms. Antifreeze Glycopeptide,Antifreeze Glycoprotein,Antifreeze Glycoproteins,Antifreeze Peptide,Antifreeze Protein,Thermal Hysteresis Protein,AFGP,Antifreeze Glycopeptides,Antifreeze Peptides,Thermal Hysteresis Proteins,Glycopeptide, Antifreeze,Glycopeptides, Antifreeze,Glycoprotein, Antifreeze,Glycoproteins, Antifreeze,Hysteresis Protein, Thermal,Hysteresis Proteins, Thermal,Peptide, Antifreeze,Peptides, Antifreeze,Protein, Antifreeze,Protein, Thermal Hysteresis,Proteins, Antifreeze,Proteins, Thermal Hysteresis

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